ProGP236 (HisJ)
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ProGP ID | ProGP236 (HisJ) |
Validation Status | Characterized |
Organism Information | |
Organism Name | Campylobacter jejuni NCTC 11168 serotype O:2 |
Domain | Bacteria |
Classification | Family: Campylobacteraceae Order: Campylobacterales Class: Epsilonproteobacteria Division or phylum: "Proteobacteria" |
Taxonomic ID (NCBI) | 192222 |
Genome Information | |
GenBank | AL111168.1 |
EMBL | AL111168 |
Organism Additional Information | Campylobacter jejuni is a microaerophilic, Gram-negative, human pathogen that is the major cause of bacterial food-borne diarrhoea (gastroenteritis). It is most frequently responsible for a form of post-infection neuromuscular paralysis known as Guillain Barre' syndrome. It also leads to an immunoproliferative small intestine disease that is a rare malignant lymphoma of the intestine. Motility is essential for pathogenicity. |
Gene Information | |
Gene Name | Cj0734c (hisJ) |
NCBI Gene ID | 905052 |
GenBank Gene Sequence | NC_002163 |
Protein Information | |
Protein Name | HisJ |
UniProtKB/SwissProt ID | Q46125 |
NCBI RefSeq | YP_002344152.1 |
EMBL-CDS | CAL34871.1 |
UniProtKB Sequence | >sp|Q46125|HISJ_CAMJE Histidine-binding protein OS=Campylobacter jejuni GN=hisJ PE=1 SV=1 MKKFLTAFLVAFTGLFLVACQNTKTENNASNEANTTLTLKVGTAPNYKPFNFKQDSKLTG FDTDLIEEIAKKNGIEIVWVETNFDGLIPALKSGKIDMIASAMSATDERRQSVDFTKPYY MSKNLYLKLKNNDSLQTKNDLEGKKIGVQLGTLQENTAKAIKNAQVQSNKDLNIAVLALK NNKIDAIVADQDTAKGFLAENPELVSFYQETDGGEGFSFAFDKNKQKDIIEIFNKGIDEA KTDGFYDTLIKKYELE |
Sequence length | 256 AA |
Subcellular Location | Periplasm |
Function | A component of the histidine uptake system. |
Glycosylation Status | |
Glycosylation Type | N- (Asn) linked |
Experimentally Validated Glycosite(s) in Full Length Protein | N29 |
Experimentally Validated Glycosite(s ) in Mature Protein | N29 |
Glycosite(s) Annotated Protein Sequence | >sp|Q46125|HISJ_CAMJE Histidine-binding protein OS=Campylobacter jejuni GN=hisJ PE=1 SV=1 MKKFLTAFLVAFTGLFLGACSDSKNKESN*(29)ASVELKVGTAPNYKPFNFKQDSKLTG FDTDLIEEIAKKNGIEIVWVETNFDGLIPALKSGKIDMIASAMSATDERRQSVDFTKPYY MSKNLYLKLKNNDSLQTKNDLEGKKIGVQLGTLQENTAKAIKNAQVQSNKDLNIAVLALK NNKIDAIVADQDTAKGFLAENPELVSFYQETDGGEGFSFAFDKNKQKDIIEIFNKGIDEA KTDGFYDTLIKKYELE |
Sequence Around Glycosites (21 AA) | ACSDSKNKESNASVELKVGTA |
Technique(s) used for Glycosylation Detection | Immunoblot analysis using glycosylation-specific R12 antiserum, SBA (soybean agglutinin) lectin-agarose affinity chromatography, Slow/ aberrant migration on SDS-PAGE |
Technique(s) used for Glycosylated Residue(s) Detection | Site-directed mutagenesis (N28L) |
Protein Glycosylation linked (PGL) gene(s) | |
OST Gene Name | PglB |
Additional Comment | Glycosylation at sequon 28-N-A-S-30 and not at the other potential sequon 132-N-D-S-134 in glycosylation competent recombinant E.coli strain as well as in native host strain suggests for the first time that N-X-S/T sequon is required but not sufficient in case of campylobacter/ bacterial N glycosylation. Seat of glycosylation was found to be periplasm. N127 is experimentally proved (by site directed mutagenesis) as non-glycosylated sequon. Sequence conflict has been observed at many places. Regarding the glycosite, it is from 18V to 38T ? GACSDSKNKESNASVE (21 residues). |
Literature | |
Year of Identification | 2005 |
Year of Identification Month Wise | 2005.4.15 |
Year of Validation | 2005 |
Reference | Maita, N., Nyirenda, J., Igura, M., Kamishikiryo, J. and Kohda, D., 2010. Comparative Structural Biology of Eubacterial and Archaeal Oligosaccharyltransferases 2. Journal of Biological Chemistry, 285(7), pp.4941-4950. |
Corresponding Author | Daisuke Kohda |
Contact | Division of Structural Biology, Medical Institute of Bioregulation, Kyushu University, Maidashi 3-1-1, Higashi-ku, Fukuoka 812-8582, Japan. |
Reference | Nita-Lazar, M., Wacker, M., Schegg, B., Amber, S. and Aebi, M., 2005. The NXS/T consensus sequence is required but not sufficient for bacterial N-linked protein glycosylation. Glycobiology, 15(4), pp.361-367. |
Corresponding Author | Markus Aebi |
Contact | Institute of Microbiology, Department of Biology, Swiss Federal Institute of Technology, Zürich, CH-8092 Zürich, Switzerland. |
Reference | Scott, N.E., Parker, B.L., Connolly, A.M., Paulech, J., Edwards, A.V., Crossett, B., Falconer, L., Kolarich, D., Djordjevic, S.P., Højrup, P. and Packer, N.H., 2011. Simultaneous glycan-peptide characterization using hydrophilic interaction chromatography and parallel fragmentation by CID, higher energy collisional dissociation, and electron transfer dissociation MS applied to the N-linked glycoproteome of Campylobacter jejuni. Molecular & cellular proteomics, 10(2), pp.S1-S18. |
Corresponding Author | Stuart J. Cordwell |
Contact | School of Molecular and Microbial Biosciences, University of Sydney, Sydney, Australia |
Reference | Maita, N., Nyirenda, J., Igura, M., Kamishikiryo, J. and Kohda, D. (2010) Comparative structural biology of eubacterial and archaeal oligosaccharyltransferases. J Biol Chem, 285, 4941-4950. [PubMed: 20007322] |
Author | Maita, N., Nyirenda, J., Igura, M., Kamishikiryo, J. and Kohda, D. |
Research Group | Institute of Microbiology, Department of Biology, Swiss Federal Institute of Technology Zurich, ETH Hönggerberg, Switzerland. |
Corresponding Author | Kohda, D |
Contact | Institute of Microbiology, Department of Biology, Swiss Federal Institute of Technology Zurich, ETH Hönggerberg, Switzerland. |
Reference | Nita-Lazar, M., Wacker, M., Schegg, B., Amber, S. and Aebi, M. (2005) The N-X-S/T consensus sequence is required but not sufficient for bacterial N-linked protein glycosylation. Glycobiology, 15, 361-367. [PubMed: 15574802] |
Author | Nita-Lazar, M., Wacker, M., Schegg, B., Amber, S. Aebi, M. |
Research Group | Institute of Microbiology, Department of Biology, Swiss Federal Institute of Technology Zurich, ETH Hönggerberg, CH-8093 Zürich, Switzerland. |
Corresponding Author | Aebi, M. |
Contact | Institute of Microbiology, Department of Biology, Swiss Federal Institute of Technology Zurich, ETH Hönggerberg, CH-8093 Zürich, Switzerland. |
Reference | Nita-Lazar, M., Wacker, M., Schegg, B., Amber, S. and Aebi, M. (2005) The N-X-S/T consensus sequence is required but not sufficient for bacterial N-linked protein glycosylation. Glycobiology, 15, 361-367. [PubMed: 15574802] |
Author | Nita-Lazar, M., Wacker, M., Schegg, B., Amber, S. Aebi, M. |
Research Group | Institute of Microbiology, Department of Biology, Swiss Federal Institute of Technology Zurich, ETH Hönggerberg, CH-8093 Zürich, Switzerland. |
Corresponding Author | Aebi, M. |
Contact | Institute of Microbiology, Department of Biology, Swiss Federal Institute of Technology Zurich, ETH Hönggerberg, CH-8093 Zürich, Switzerland. |
Reference | Scott NE, Parker BL, Connolly AM, Paulech J, Edwards AV, Crossett B, Falconer L, Kolarich D, Djordjevic SP, Højrup P, Packer NH, Larsen MR, Cordwell SJ. (2011) Simultaneous glycan-peptide characterization using hydrophilic interaction chromatography and parallel fragmentation by CID, higher energy collisional dissociation, and electron transfer dissociation MS applied to the N-linked glycoproteome of Campylobacter jejuni. Mol Cell Proteomics, 10(2), M000031-MCP201. [PubMed: 20360033] |
Author | Scott NE, Parker BL, Connolly AM, Paulech J, Edwards AV, Crossett B, Falconer L, Kolarich D, Djordjevic SP, Højrup P, Packer NH, Larsen MR, Cordwell SJ |
Research Group | School of Molecular and Microbial Biosciences, University of Sydney, Sydney, Australia |
Corresponding Author | Cordwell SJ |
Contact | School of Molecular and Microbial Biosciences, University of Sydney, Sydney, Australia |